This invention relates to plasminogen activators which are useful thrombolytic agents. More particularly, this invention relates to glycosylated tissue plasminogen activator from cultured normal human colon cells.
In copending application Ser. No. 929,950, filed Nov. 11, 1986, now U.S. Pat. No. 4,751,084, a novel tissue plasminogen activator (t-PA) is disclosed which has a unique glycosylation pattern and which is derived from normal human colon fibroblast cells.
A group of sixteen different oligosaccharides were identified and characterized as forming part of the sugar moiety of the glycoprotein.
The normal human colon fibroblast t-PA was further characterized in terms of the Type I and Type II glycoforms. In Type I the t-PA protein moiety of 527 amino acids is glycosylated at Asn-117, Asn-184 and Asn-448; whereas, in Type II the glycosylation occurs at Asn-117 and Asn-184. The relative incidence of complex, hybrid and oligomannose structures in each of the Type I and Type II t-PA glycoproteins is shown.